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HDAC5 Controls MEF2C-Driven Sclerostin Expression in Osteocytes
Open accessAbstract
Osteocytes secrete paracrine factors that regulate the balance between bone formation and destruction. Among these molecules, sclerostin (encoded by the gene SOST) inhibits osteoblastic bone formation and is an osteoporosis drug target. The molecular mechanisms underlying SOST expression remain largely unexplored. Here, we report that histone deacetylase 5 (HDAC5) negatively regulates sclerostin levels in osteocytes in vitro and in vivo. HDAC5 shRNA increases, whereas HDAC5 overexpression decreases SOST expression in the novel murine Ocy454 osteocytic cell line. HDAC5 knockout mice show increased levels of SOST mRNA, more sclerostin-positive osteocytes, decreased Wnt activity, low trabecular bone density, and reduced bone formation by osteoblasts. In osteocytes, HDAC5 binds and inhibits the function of MEF2C, a crucial transcription factor for SOST expression. Using chromatin immunoprecipitation, we have mapped endogenous MEF2C binding in the SOST gene to a distal intergenic enhancer 45 kB downstream from the transcription start site. HDAC5 deficiency increases SOST enhancer MEF2C chromatin association and H3K27 acetylation and decreases recruitment of corepressors NCoR and HDAC3. HDAC5 associates with and regulates the transcriptional activity of this enhancer, suggesting direct regulation of SOST gene expression by HDAC5 in osteocytes. Finally, increased sclerostin production achieved by HDAC5 shRNA is abrogated by simultaneous knockdown of MEF2C, indicating that MEF2C is a major target of HDAC5 in osteocytes. © 2014 American Society for Bone and Mineral Research.
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“Recently, Sato et al.20,44 showed that FFSS induces the disruption of the FAK-integrin complex, thereby inhibiting histone deacetylase 4/5 (HDAC4/5), a negative regulator of SOST expression in osteocytes45 modulated by parathyroid hormone (PTH) treatment.46”
From Bone remodeling: an operational process ensuring survival and bone mechanical competence (2022) · cites this paper as [45]
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Choudhary, C., Kumar, C., Gnad, F., Nielsen, M. L., Rehman, M., Walther, T. C., Olsen, J. V., & Mann, M. (2009) · Science · doi:10.1126/science.1175371 · Cited by 4,040
Haberland, M., Montgomery, R. L., & Olson, E. N. (2008) · Nature Reviews Genetics · doi:10.1038/nrg2485 · Cited by 2,600
Bonewald, L. F. (2011) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.320 · Cited by 2,287
Control of β-Catenin Phosphorylation/Degradation by a Dual-Kinase Mechanism
Liu, C., Li, Y., Semënov, M. V., Han, C., Baeg, G., Tan, Y., Zhang, Z., Lin, X., & He, X. (2002) · Cell · doi:10.1016/s0092-8674(02)00685-2 · Cited by 2,152
WNT signaling in bone homeostasis and disease: From human mutations to treatments
Baron, R., & Kneissel, M. (2013) · Nature Medicine · doi:10.1038/nm.3074 · Cited by 2,093
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Moffat, J., Grueneberg, D. A., Yang, X., Kim, S. Y., Kloepfer, A. M., Hinkle, G., Piqani, B., Eisenhaure, T., Luo, B., Grenier, J. K., et al. (2006) · Cell · doi:10.1016/j.cell.2006.01.040 · Cited by 1,804
Self-citationEvidence for osteocyte regulation of bone homeostasis through RANKL expression
Nakashima, T., Hayashi, M., Fukunaga, T., Kurata, K., Oh-hora, M., Feng, J. Q., Bonewald, L. F., Kodama, T., Wutz, A., Wagner, E. F., et al. (2011) · Nature Medicine · doi:10.1038/nm.2452 · Cited by 1,778
ChIP-seq accurately predicts tissue-specific activity of enhancers
Visel, A., Blow, M. J., Li, Z., Zhang, T., Akiyama, J. A., Holt, A., Plajzer-Frick, I., Shoukry, M., Wright, C., Chen, F., et al. (2009) · Nature · doi:10.1038/nature07730 · Cited by 1,639
Mechanical Stimulation of Bone in Vivo Reduces Osteocyte Expression of Sost/Sclerostin
Robling, A. G., Niziolek, P. J., Baldridge, L. A., Condon, K. W., Allen, M. R., Alam, I., Mantila, S. M., Gluhak-Heinrich, J., Bellido, T. M., Harris, S. E., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m705092200 · Cited by 1,350
Matrix-embedded cells control osteoclast formation
Xiong, J., Onal, M., Jilka, R. L., Weinstein, R. S., Manolagas, S. C., & O'Brien, C. A. (2011) · Nature Medicine · doi:10.1038/nm.2448 · Cited by 1,304
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Maeda, K., Kobayashi, Y., Koide, M., Uehara, S., Okamoto, M., Ishihara, A., Kayama, T., Saito, M., & Marumo, K. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20225525 · Cited by 360
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Spatz, J., Wein, M. N., Gooi, J. H., Qu, Y., Garr, J., Liu, X. S., Barry, K. J., Uda, Y., Lai, F., Dedic, C., et al. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.628313 · Cited by 304
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Wein, M. N., & Kronenberg, H. M. (2018) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a031237 · Cited by 257
Self-citationThe chronic kidney disease — Mineral bone disorder (CKD-MBD): Advances in pathophysiology
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SIKs control osteocyte responses to parathyroid hormone
Wein, M. N., Liang, Y., Göransson, O., Sundberg, T. B., Wang, J., Williams, E. A., O’Meara, M. J., Govea, N., Beqo, B., Nishimori, S., et al. (2016) · Nature Communications · doi:10.1038/ncomms13176 · Cited by 163
Self-citationHistone Deacetylases in Bone Development and Skeletal Disorders
Bradley, E. W., Shull, L. C., van Wijnen, A. J., McGee‐Lawrence, M. E., & Westendorf, J. J. (2015) · Physiological Reviews · doi:10.1152/physrev.00004.2015 · Cited by 163
Sclerostin's role in bone's adaptive response to mechanical loading
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Self-citationFulzele, K. S., Lai, F., Dedic, C., Saini, V., Uda, Y., Shi, C., Tuck, P., Aronson, J., Liu, X., Spatz, J., et al. (2016) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.3001 · Cited by 102
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Lei, H., He, M., He, X., Li, G., Wang, Y., Gao, Y., Yan, G., Wang, Q., Li, T., Liu, G., et al. (2021) · PubMed Central · Cited by 42
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Self-citationJohn, H. C. S., Meyer, M. B., Benkusky, N. A., Carlson, A. H., Prideaux, M., Bonewald, L. F., & Pike, J. W. (2014) · Bone · doi:10.1016/j.bone.2014.11.010 · Cited by 39
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Ramaswamy, G., Kim, H., Zhang, D., Lounev, V. Y., Wu, J. Y., Choi, Y., Kaplan, F. S., Pignolo, R. J., & Shore, E. M. (2017) · Scientific Reports · doi:10.1038/srep45140 · Cited by 36
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Meng, X.-H., Chen, X., Greenbaum, J., Zeng, Q., You, S.-L., Xiao, H., Tan, L., & Deng, H. (2018) · Bone · doi:10.1016/j.bone.2018.05.012 · Cited by 30
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Self-citation
Metadata
- Authors
- Wein, M. N., Spatz, J., Nishimori, S., Doench, J., Root, D., Babij, P., Nagano, K., Baron, R., Brooks, D., Bouxsein, M., Pajevic, P. D., & Kronenberg, H. M.
- Affiliations
- Massachusetts General Hospital (US)
- Broad Institute (US)
- Amgen (United States) (US)
- Harvard University (US)
- Corresponding author
- Kronenberg, Henry M
- ORCID
- Venue
- Journal of Bone and Mineral Research
- Publisher
- Oxford University Press (OUP)
- Published
- 2014-10-01
- Volume
- 30
- Issue
- 3
- Pages
- 400-411
- ISSN
- 0884-0431 (ISSN-L)
- 1523-4681
- PMC
- PMC4342334
- OpenAlex
- W2151454340
- Cited by
- 158
- References
- 64
- Citations by year
- 2026: 11 · 2025: 6 · 2024: 7 · 2023: 10 · 2022: 12 · 2021: 17 · 2020: 18 · 2019: 14 · 2018: 10 · 2017: 25 · 2016: 15 · 2015: 11 · 2014: 2
- FWCI
- 7.25
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model (vor)
- Locations
- Journal of Bone and Mineral Research (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Institutional Repositories DataBase (IRDB) (submittedVersion)
- Funders
- National Institute of Diabetes and Digestive and Kidney Diseases (P01DK11794, P01DK011794, F32DK100215, T32DK007028)
- National Institute of Arthritis and Musculoskeletal and Skin Diseases (UH3AR059655)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Bone Metabolism and Diseases
- Health Sciences › Medicine › Orthopedics and Sports Medicine › Bone health and osteoporosis research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
- Keywords
- HDAC5, sclerostin, MEF2C, osteocytes, histone deacetylase, transcriptional regulation, enhancers, Wnt signaling, bone formation, osteoporosis, H3K27 acetylation, NCoR, HDAC3, chromatin binding
- MeSH terms
- Animals, Glycoproteins, Histone Deacetylases, Osteocytes, Mice, Knockout, Intercellular Signaling Peptides and Proteins, Adaptor Proteins, Signal Transducing, Mice, MEF2 Transcription Factors
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